Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor, and characterization of the gene and its product

Applied and Environmental Microbiology

Volumn 62, Issue 7, 1996, Pages 2303-2310

  Kita, Keiko ^a   Matsuzaki, Koji ^a   Hashimoto, Tetsu ^a   Yanase, Hideshi ^a   Kato, Nobuo ^a,c   Chung, Max Ching Ming ^b   Kataoka, Michihiko ^c   Shimizu, Sakayu ^c  

^a TOTTORI UNIVERSITY   (Japan)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^c KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; FUNGAL PROTEIN; GENE PRODUCT;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; FUNGAL GENETICS; GENE SEQUENCE; MOLECULAR CLONING; NONHUMAN; YEAST;

ESCHERICHIA COLI; SPORIDIOBOLUS SALMONICOLOR;

EID: 0029959335     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.62.7.2303-2310.1996     Document Type: Article

References (35)

1. Amore, R., P. Kötter, C. Kuster, M. Ciriacy, and C. P. Hollenberg. 1991. Cloning and expression in Saccharomyces cerevisiae of the NAD(P)H-dependent xylose reductase-encoding gene (XYL1) from the xylose-assimilating yeast Pichia stipitis. Gene 109:89-97.
2. Bartels, D., K. Engelhardt, R. Roncarati, K. Schneider, M. Rotter, and F. Salamani. 1991. An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein. EMBO J. 10:1037-1043.
3. Bohren, K. M., B. Bullock, B. Wermuth, and K. H. Gabbay. 1989. The aldo-keto reductase superfamily. J. Biol. Chem. 264:9547-9551.
4. Bohren, K. M., C. E. Grimshaw, C.-J. Lai, D. H. Harrison, D. G. Ringe, A. Petsko, and K. H. Gabbay. 1994. Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 33:2021-2032.
5. Bohren, K. M., J. L. Page, R. Shankar, S. P. Henry, and K. H. Gabbay. 1991. Expression of human aldose and aldehyde reductases. J. Biol. Chem. 266: 24031-24037.
6. Borhani, D. W., T. M. Harter, and J. M. Petrash. 1992. The crystal structure of the aldose reductase : NADPH binary complex. J. Biol. Chem. 267:24841-24847.
7. Brosius, J., and A. Holy. 1984. Regulation of ribosomal RNA promoter with a synthetic lac operator. Proc. Natl. Acad. Sci. USA 81:6929-6933.
8. Carper, D., C. Nishimura, T. Shinohara, B. Dietzchold, G. Wistow, C. Craft, P. Kador, and J. H. Kinoshita. 1987. Aldose reductase and p-crystallin belong to the same protein superfamily as aldehyde reductase. FEBS Lett. 220:209-213.
9. Fujii, Y., K. Watanabe, H. Hayashi, Y. Urade, S. Kuramitsu, H. Kagamiyama, and O. Hayaishi. 1990. Purification and characterization of ρ-crystallin from Japanese common bullfrog lens. J. Biol. Chem. 265:9914-9923.
10. Garcia-Perez, A., B. Martin, H. R. Murphy, S. Uchida, H. Murer, B. D. Cowley, Jr., J. S. Handler, and M. B. Burg. 1989. Molecular cloning of cDNA coding for kidney aldose reductase. J. Biol. Chem. 264:16815-16821.
11. Graham, A., L. Brown, P. J. Hedge, A. J. Gammack, and A. F. Markham. 1991. Structure of the human aldose reductase gene. J. Biol. Chem. 266: 6872-6877.
12. Grindley, J. F., M. A. Payton, H. Van De Pol, and K. G. Hardy. 1988. Conversion of glucose to 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a recombinant strain of Erwinia citreus. Appl. Environ. Microbiol. 54:1770-1775.
13. Kataoka, M., H. Sakai, T. Morikawa, M. Katoh, T. Miyoshi, S. Shimizu, and H. Yamada. 1992. Characterization of aldehyde reductase of Sporobolomyces salmonicolor. Biochim. Biophys. Acta 1122:57-62.
14. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
15. Messing, J., and J. Vieira. 1982. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene 19:269-276.
16. Oechsner, U., V. Magdolen, and W. Bandlow. 1988. A nuclear yeast gene (GCY) encodes a polypeptide with high homology to a vertebrate eye lens protein. FEBS Lett. 238:123-128.
17. Onishi, Y., M. Noshiro, T. Shimosato, and K. Okuda. 1991. Molecular cloning and sequence analysis of cDNA encoding delta(4)-3-ketosteroid 5-beta-reductase of rat liver. FEBS Lett. 283:215-218.
18. Padgett, R. A., P. J. Grabowski, M. M. Konarska, S. Seiler, and P. A. Sharp. 1986. Splicing of messenger RNA precursors. Annu. Rev. Biochem. 55:1119-1150.
19. Pailhoux, E. A., A. Martinez, G. M. Veyssiere, and C. G. Jean. 1990. Androgen-dependent protein from mouse vas deferens. J. Biol. Chem. 265:19932-19936.
20. Rondeau, J. M., F. Tete-Favier, A. Podjarny, J. M. Reymann, P. Barth, J. F. Biellmann, and D. Moras. 1992. Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature (London) 355:469-472.
21. Samaras, N., and T. W. Spithill. 1989. The developmentally regulated p100/ 11E gene of Leishmania major shows homology to a superfamily of reductase genes. J. Biol. Chem. 264:4251-4254.
22. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
23. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
24. Schade, S. Z., S. L. Early, T. R. Williams, F. J. Kezdy, R. L. Heinrikson, C. E. Grimshaw, and C. C. Doughty. 1990. Sequence analysis of bovine lens aldose reductase. J. Biol. Chem. 265:3628-3635.
25. Sherman, F., G. R. Fink, and J. B. Hicks. 1986. Laboratory course manual for methods in yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
26. Shine, J., and L. Dalgarno. 1974. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71:1342-1346.
27. Shiraishi, A., and H. Fujii. 1978. Sporobolomyces cell wall lytic enzyme produced by a bacterium, no. 98. Nippon Nogeikagaku Kaishi 52:553-559. (In Japanese.)
28. Tarle, I., D. Borhani, W. D. K. Wilson, F. A. Quiocho, and J. M. Petrash. 1993. Probing the active site of human aldose reductase. J. Biol. Chem. 268:25687-25693.
29. Watanabe, K., Y. Fujii, K. Nakayama, H. Ohkubo, S. Kuramitsu, H. Kagamiyama, S. Nakanishi, and O. Hayaishi. 1988. Structural similarity of bovine lung prostaglandin F synthase to lens ε-crystallin of the European common frog. Proc. Natl. Acad. Sci. USA 85:11-15.
30. Welle, R., G. Schröder, E. Schiltz, H. Grisebach, and J. Schröder. 1991. Induced plant responses to pathogen attack. Eur. J. Biochem. 196:423-430.
31. Wermuth, B., H. Burgisser, K. Bohren, and J.-P. Von Wartburg. 1982. Purification and characterization of human-brain aldose reductase. Eur. J. Biochem. 127:279-284.
32. Wermuth, B., J. D. B. Munch, and J.-P. Von Wartburg. 1977. Purification and properties of NADPH-dependent aldehyde reductase from human liver. J. Biol. Chem. 252:3821-3828.
33. Wilson, D. K., K. M. Bohren, K. H. Gabbay, and F. A. Quiocho. 1992. An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81-84.
34. Winters, C. J., D. T. Molowa, and P. S. Guzelian. 1990. Isolation and characterization of cloned cDNA encoding human liver chlordecone reductase. Biochemistry 29:1080-1087.
35. Yamada, H., S. Shimizu, M. Kataoka, H. Sakai, and T. Mijoshi. 1990. A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of β-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization. FEMS Microbiol. Lett. 70:45-48.